2005
DOI: 10.1042/bj20041931
|View full text |Cite
|
Sign up to set email alerts
|

LEA proteins prevent protein aggregation due to water stress

Abstract: LEA (late embryogenesis abundant) proteins in both plants and animals are associated with tolerance to water stress resulting from desiccation and cold shock. However, although various functions of LEA proteins have been proposed, their precise role has not been defined. Recent bioinformatics studies suggest that LEA proteins might behave as molecular chaperones, and the current study was undertaken to test this hypothesis. Recombinant forms of AavLEA1, a group 3 LEA protein from the anhydrobiotic nematode Aph… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

20
576
3
8

Year Published

2007
2007
2023
2023

Publication Types

Select...
6
3
1

Relationship

0
10

Authors

Journals

citations
Cited by 714 publications
(607 citation statements)
references
References 45 publications
20
576
3
8
Order By: Relevance
“…Additionally, sweetie shows altered expression for late embryogenesis-abundant (LEA) genes and many DREB2-type TFs. LEAs are anti-aggregation proteins that together with trehalose protect plant cells during the dehydration typical of abiotic stresses such as cold and drought 53 , whereas DREB2A and DREB2B are key transcription factors regulating responses to dehydration and high-salinity stresses 54 . In birch, DREB TFs have been associated with cold acclimation and winter hardiness 55 .…”
Section: Candidate Gene Adaptation Correlates With Environmentmentioning
confidence: 99%
“…Additionally, sweetie shows altered expression for late embryogenesis-abundant (LEA) genes and many DREB2-type TFs. LEAs are anti-aggregation proteins that together with trehalose protect plant cells during the dehydration typical of abiotic stresses such as cold and drought 53 , whereas DREB2A and DREB2B are key transcription factors regulating responses to dehydration and high-salinity stresses 54 . In birch, DREB TFs have been associated with cold acclimation and winter hardiness 55 .…”
Section: Candidate Gene Adaptation Correlates With Environmentmentioning
confidence: 99%
“…Although prevalent in desiccated seeds, they decrease significantly once germination begins [25]. They are characterised by being rich in hydrophilic amino acids (such as lysine and glycine) ordered in repeated sequences [28], which results in hydrophilic side chains that are thought to interact with, and protect hydrophilic proteins during desiccation by causing aggregation [29]. In an attempt to further understand this diverse group of proteins they have been categorised on the basis of the presence or absence of specific sequence motifs [30].…”
Section: Discussionmentioning
confidence: 99%
“…Structural shifts such as superhelical filamentous, coiled coil like structures in group 3a (SF2) and other categories of LEA proteins depend on the availability of water suggesting that LEAs may form part of the cytoskeleton (Wise and Tunnacliffe, 2004). However, recent studies indicate that LEA proteins do not behave as classical molecular chaperones but nevertheless do exhibit protective synergistic effect in the presence of trehalose suggesting the likelihood of its functioning as a molecular shield towards preventing the formation of damaged protein aggregates (Goyal et al, 2005). Blackman et al (1995) observed that in ABA-treated immature embryo axes, despite having high levels of LEA-like proteins, the electrolyte leakage was noticeably higher than that of the mature desiccation tolerant embryo axes and therefore surmised that the protection conferred by the LEAs might be during the recovery phase.…”
Section: Lea Proteinsmentioning
confidence: 99%